Mass-Spectrometry Based Characterisation of Infant Whole Saliva Peptidome

The objective of the study was to determine optimal conditions for sampling, sample processing and mass-spectrometry based analysis of infants’ salivary peptidome. Saliva was sampled in 3- and 6-month-old infants and peptide extracts were prepared. Various sample pretreatments before profiling by MA...

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Bibliographic Details
Published inInternational Journal of Peptide Research and Therapeutics Vol. 15; no. 3; pp. 177 - 185
Main Authors Lucchi, G., Chambon, C., Truntzer, C., Pecqueur, D., Ducoroy, P., Schwartz, C., Nicklaus, S., Morzel, M.
Format Journal Article
LanguageEnglish
Published Dordrecht Springer Netherlands 01.09.2009
Springer Nature B.V
Springer Verlag
Subjects
Animal Anatomy
Babies
Biochemistry
Biomedical and Life Sciences
Body fluids
Chemical and Process Engineering
Engineering Sciences
Food engineering
Histology
Life Sciences
Mass spectrometry
Molecular Medicine
Morphology
Peptides
Pharmaceutical Sciences/Technology
Pharmacology/Toxicology
Polymer Sciences
Proteins
PRPs
Infants
MALDI-ToF
Sample pretreatment
Mass spectrometry
Saliva peptidome
PRPS
MASS SPECTROMETRY
SAMPLE PRETREATMENT
MALDI-TOF
SALIVA PEPTIDOME
INFANTS
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Summary:The objective of the study was to determine optimal conditions for sampling, sample processing and mass-spectrometry based analysis of infants’ salivary peptidome. Saliva was sampled in 3- and 6-month-old infants and peptide extracts were prepared. Various sample pretreatments before profiling by MALDI-ToF were evaluated and peptide identification was undertaken by MALDI-ToF/ToF or nanoLC-ESI-IT tandem MS. A fast and simple protocol (cut-off filtration at 5 kDa) was satisfactory to produce extracts where no proteolysis was detected even when no protease inhibitor was added. Optimal MALDI spectra were generated after purification on C18 tips. Variability of spectra between two samples exceeded that of the technical replicates, validating that the method is suitable to conduct differential studies. Salivary peptides, identified by means of the two complementary mass spectrometry techniques, were fragments of proline-rich proteins and histatins. The fragments originated mainly from the C-terminal protein extremities. Indications on the proteolytic systems involved and the anatomic location where they intervene are proposed.
ISSN:1573-3149
1573-3904
1573-496X
DOI:10.1007/s10989-009-9167-2